STRINGSTRING
pflB pflB adhE adhE adhP adhP pta pta eutG eutG eutE eutE fucO fucO yiaY yiaY frdC frdC frdB frdB ahr ahr bcsZ bcsZ lacI lacI
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
pflBFormate acetyltransferase 1; Protein involved in anaerobic respiration and cellular amino acid catabolic process. (760 aa)
adhEAcetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. (891 aa)
adhPEthanol-active dehydrogenase/acetaldehyde-active reductase; Preferred specificity is towards 1-propanol; Belongs to the zinc-containing alcohol dehydrogenase family. (336 aa)
ptaPhosphate acetyltransferase; Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. In the N-terminal section; belongs to the CobB/CobQ family. (714 aa)
eutGEthanol dehydrogenase involved in ethanolamine utilization; May act on the acetaldehyde produced from the degradation of ethanolamine; Belongs to the iron-containing alcohol dehydrogenase family. (395 aa)
eutEAldehyde oxidoreductase, ethanolamine utilization protein; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. (467 aa)
fucOL-1,2-propanediol oxidoreductase; Protein involved in carbohydrate catabolic process and glycolate metabolic process; Belongs to the iron-containing alcohol dehydrogenase family. (382 aa)
yiaYL-threonine dehydrogenase; Putative oxidoreductase. (383 aa)
frdCFumarate reductase (anaerobic), membrane anchor subunit; Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. (131 aa)
frdBFumarate reductase (anaerobic), Fe-S subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. (244 aa)
ahrBroad specificity NADPH-dependent aldehyde reductase, Zn-containing; Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined. (339 aa)
bcsZendo-1,4-D-glucanase; Hydrolyzes carboxymethylcellulose. (368 aa)
lacILactose-inducible lac operon transcriptional repressor; Repressor of the lactose operon. Binds allolactose as an inducer. (360 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.